2V17
Structure of the complex of antibody MN423 with a fragment of tau protein
Experimental procedure
| Experimental method | SINGLE WAVELENGTH |
| Source type | SYNCHROTRON |
| Source details | EMBL/DESY, HAMBURG BEAMLINE BW7B |
| Synchrotron site | EMBL/DESY, HAMBURG |
| Beamline | BW7B |
| Temperature [K] | 100 |
| Detector technology | IMAGE PLATE |
| Collection date | 2006-02-10 |
| Detector | MARRESEARCH |
| Spacegroup name | P 1 21 1 |
| Unit cell lengths | 71.541, 36.808, 85.543 |
| Unit cell angles | 90.00, 113.93, 90.00 |
Refinement procedure
| Resolution | 79.060 - 1.650 |
| R-factor | 0.16 |
| Rwork | 0.156 |
| R-free | 0.21800 |
| Structure solution method | MOLECULAR REPLACEMENT |
| Starting model (for MR) | 1nbv |
| RMSD bond length | 0.016 |
| RMSD bond angle | 1.663 |
| Data reduction software | DENZO |
| Data scaling software | SCALEPACK |
| Phasing software | MOLREP |
| Refinement software | REFMAC (5.1.24) |
Data quality characteristics
| Overall | Outer shell | |
| Low resolution limit [Å] | 20.000 | 1.680 |
| High resolution limit [Å] | 1.650 | 1.650 |
| Rmerge | 0.070 | 0.280 |
| Number of reflections | 49464 | |
| <I/σ(I)> | 20.1 | 3.7 |
| Completeness [%] | 99.8 | 99.2 |
| Redundancy | 3.6 | 3.3 |
Crystallization Conditions
| crystal ID | method | pH | temperature | details |
| 1 | 7.5 | CRYSTALS WERE GROWN FROM 3 UL DROPS CONTAINING 10MG/ML OF PROTEIN, 15 % PEG1000, 100MM HEPES, PH 7.2 |
